Novel inhibitor cystine knot peptides from Momordica charantia.

Two new peptides, MCh-1 and MCh-2, along with three known trypsin inhibitors (MCTI-I, MCTI-II and MCTI-III), were isolated from the seeds of the tropical vine Momordica charantia. The sequences of the peptides were determined using mass spectrometry and NMR spectroscopy. Using a strategy involving p...

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Autores principales:	Wen-Jun He, Lai Yue Chan, Richard J Clark, Jun Tang, Guang-Zhi Zeng, Octavio L Franco, Cinzia Cantacessi, David J Craik, Norelle L Daly, Ning-Hua Tan
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/25dff0e106de40bc8b81b9d0147e0a41
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spelling	oai:doaj.org-article:25dff0e106de40bc8b81b9d0147e0a412021-11-18T08:51:57ZNovel inhibitor cystine knot peptides from Momordica charantia.1932-620310.1371/journal.pone.0075334https://doaj.org/article/25dff0e106de40bc8b81b9d0147e0a412013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24116036/?tool=EBIhttps://doaj.org/toc/1932-6203Two new peptides, MCh-1 and MCh-2, along with three known trypsin inhibitors (MCTI-I, MCTI-II and MCTI-III), were isolated from the seeds of the tropical vine Momordica charantia. The sequences of the peptides were determined using mass spectrometry and NMR spectroscopy. Using a strategy involving partial reduction and stepwise alkylation of the peptides, followed by enzymatic digestion and tandem mass spectrometry sequencing, the disulfide connectivity of MCh-1 was elucidated to be CysI-CysIV, CysII-CysV and CysIII-CysVI. The three-dimensional structures of MCh-1 and MCh-2 were determined using NMR spectroscopy and found to contain the inhibitor cystine knot (ICK) motif. The sequences of the novel peptides differ significantly from peptides previously isolated from this plant. Therefore, this study expands the known peptide diversity in M. charantia and the range of sequences that can be accommodated by the ICK motif. Furthermore, we show that a stable two-disulfide intermediate is involved in the oxidative folding of MCh-1. This disulfide intermediate is structurally homologous to the proposed ancestral fold of ICK peptides, and provides a possible pathway for the evolution of this structural motif, which is highly prevalent in nature.Wen-Jun HeLai Yue ChanRichard J ClarkJun TangGuang-Zhi ZengOctavio L FrancoCinzia CantacessiDavid J CraikNorelle L DalyNing-Hua TanPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 10, p e75334 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Wen-Jun He Lai Yue Chan Richard J Clark Jun Tang Guang-Zhi Zeng Octavio L Franco Cinzia Cantacessi David J Craik Norelle L Daly Ning-Hua Tan Novel inhibitor cystine knot peptides from Momordica charantia.
description	Two new peptides, MCh-1 and MCh-2, along with three known trypsin inhibitors (MCTI-I, MCTI-II and MCTI-III), were isolated from the seeds of the tropical vine Momordica charantia. The sequences of the peptides were determined using mass spectrometry and NMR spectroscopy. Using a strategy involving partial reduction and stepwise alkylation of the peptides, followed by enzymatic digestion and tandem mass spectrometry sequencing, the disulfide connectivity of MCh-1 was elucidated to be CysI-CysIV, CysII-CysV and CysIII-CysVI. The three-dimensional structures of MCh-1 and MCh-2 were determined using NMR spectroscopy and found to contain the inhibitor cystine knot (ICK) motif. The sequences of the novel peptides differ significantly from peptides previously isolated from this plant. Therefore, this study expands the known peptide diversity in M. charantia and the range of sequences that can be accommodated by the ICK motif. Furthermore, we show that a stable two-disulfide intermediate is involved in the oxidative folding of MCh-1. This disulfide intermediate is structurally homologous to the proposed ancestral fold of ICK peptides, and provides a possible pathway for the evolution of this structural motif, which is highly prevalent in nature.
format	article
author	Wen-Jun He Lai Yue Chan Richard J Clark Jun Tang Guang-Zhi Zeng Octavio L Franco Cinzia Cantacessi David J Craik Norelle L Daly Ning-Hua Tan
author_facet	Wen-Jun He Lai Yue Chan Richard J Clark Jun Tang Guang-Zhi Zeng Octavio L Franco Cinzia Cantacessi David J Craik Norelle L Daly Ning-Hua Tan
author_sort	Wen-Jun He
title	Novel inhibitor cystine knot peptides from Momordica charantia.
title_short	Novel inhibitor cystine knot peptides from Momordica charantia.
title_full	Novel inhibitor cystine knot peptides from Momordica charantia.
title_fullStr	Novel inhibitor cystine knot peptides from Momordica charantia.
title_full_unstemmed	Novel inhibitor cystine knot peptides from Momordica charantia.
title_sort	novel inhibitor cystine knot peptides from momordica charantia.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/25dff0e106de40bc8b81b9d0147e0a41
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Novel inhibitor cystine knot peptides from Momordica charantia.

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